1993
Calmodulin-binding domain of recombinant erythrocyte beta-adducin.
Scaramuzzino D, Morrow J. Calmodulin-binding domain of recombinant erythrocyte beta-adducin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3398-3402. PMID: 8475088, PMCID: PMC46307, DOI: 10.1073/pnas.90.8.3398.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesBlood ProteinsCalmodulinCalmodulin-Binding ProteinsCalpainCattleCloning, MolecularDNAErythrocytesKineticsMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesPhosphorylationProtein Structure, SecondaryRecombinant ProteinsRestriction MappingTrypsinConceptsCaM-binding activityBeta-adducinBundles F-actinProtease-sensitive domainsCAMP-dependent kinaseCaM-binding domainPartial cDNA cloneBinding of spectrinAmino acid codeDependent CaM bindingProtein kinase CSingle letter amino acid codeCaM-binding sequenceProtease-resistant corePEST sequenceCovalent phosphorylationShares structural featuresCDNA clonesCortical cytoskeletonHeterodimeric proteinStructural basisConsensus sequenceMammalian erythrocytesProtease sensitivityBind calmodulin
1990
Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions
BECKER P, SCHWARTZ M, MORROW J, Samuel E. Radiolabel‐transfer cross‐linking demonstrates that protein 4.1 binds to the N‐terminal region of β spectrin and to actin in binary interactions. The FEBS Journal 1990, 193: 827-836. PMID: 2249696, DOI: 10.1111/j.1432-1033.1990.tb19406.x.Peer-Reviewed Original Research
1988
Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site
Harris A, Morrow J. Proteolytic processing of human brain alpha spectrin (fodrin): identification of a hypersensitive site. Journal Of Neuroscience 1988, 8: 2640-2651. PMID: 3074159, PMCID: PMC6569499, DOI: 10.1523/jneurosci.08-07-02640.1988.Peer-Reviewed Original ResearchConceptsLong-term potentiationBrain spectrinCalcium-dependent mechanismCalcium-dependent neutral proteaseCalcium-dependent proteaseCentral molecular mechanismsSite of actionReceptor functionPostsynaptic membraneCalcium-dependent mannerFurther investigationMolecular mechanismsGel overlay techniqueAlpha subunitNeutral proteaseNonerythroid spectrinImportant moleculesProteolytic processingCleavage fragmentsPotentiationProtease
1986
A calmodulin and α-subunit binding domain in human erythrocyte spectrin
Sears D, Marchesi V, Morrow J. A calmodulin and α-subunit binding domain in human erythrocyte spectrin. Biochimica Et Biophysica Acta 1986, 870: 432-442. PMID: 3697360, DOI: 10.1016/0167-4838(86)90251-7.Peer-Reviewed Original ResearchConceptsCalmodulin binding siteSpectrin-actin membrane skeletonBinding sitesSubunit-subunit associationMr fragmentTwo-dimensional peptide mappingPutative calmodulin binding siteErythrocyte spectrinNon-erythroid spectrinCleavage of spectrinHuman erythrocyte spectrinProtein 4.1Cyanogen bromide cleavageMembrane skeletonActin bindingCalmodulin bindingNH2 terminusBind calmodulinNative conditionsBeta subunitCalmodulin regulationTerminal regionSpectrinPeptide mappingCalmodulinMechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin
Harris A, Anderson J, Yurchenco P, Green L, Ainger K, Morrow J. Mechanisms of cytoskeletal regulation: Functional and antigenic diversity in human erythrocyte and brain beta spectrin. Journal Of Cellular Biochemistry 1986, 30: 51-69. PMID: 2420811, DOI: 10.1002/jcb.240300107.Peer-Reviewed Original ResearchAbnormal spectrin in hereditary elliptocytosis.
Marchesi S, Knowles W, Morrow J, Bologna M, Marchesi V. Abnormal spectrin in hereditary elliptocytosis. Blood 1986, 67: 141-51. PMID: 3940543, DOI: 10.1182/blood.v67.1.141.bloodjournal671141.Peer-Reviewed Original ResearchConceptsClinical expressionHemolytic anemiaSubset of patientsRare hemolytic anemiaAlpha iAlpha II domainAlpha subunitHereditary pyropoikilocytosisFunctional resultsSpectrin alpha subunitHereditary elliptocytosisHematologic diseasesAnemiaMild elliptocytosisAbnormal spectrinSeverityPresent studyKD peptideExpressionD-peptidesFrequent occurrenceSpectrin self-association
1983
Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis.
Knowles W, Morrow J, Speicher D, Zarkowsky H, Mohandas N, Mentzer W, Shohet S, Marchesi V. Molecular and functional changes in spectrin from patients with hereditary pyropoikilocytosis. Journal Of Clinical Investigation 1983, 71: 1867-1877. PMID: 6863544, PMCID: PMC370392, DOI: 10.1172/jci110942.Peer-Reviewed Original Research
1982
A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains.
Speicher D, Morrow J, Knowles W, Marchesi V. A structural model of human erythrocyte spectrin. Alignment of chemical and functional domains. Journal Of Biological Chemistry 1982, 257: 9093-9101. PMID: 7096353, DOI: 10.1016/s0021-9258(18)34247-9.Peer-Reviewed Original ResearchConceptsNumerous small peptidesPeptide mapping techniquesChemical domainsPeptide segmentsMolecular weightChemical cleavageSized peptidesTwo-dimensional peptide mapping techniquesSmall peptidesIntact moleculeUnique peptidesPhosphorylated amino acidsFurther proteolytic cleavageOverlap peptidesPolypeptide segmentsIntermediate-sized peptidesMoleculesMild trypsin digestionTrypsin digestionTwo-dimensional peptide mapsPeptidesStructural modelSpectrin subunitsCleavagePeptide mapsMonoclonal antibodies as probes of domain structure of the spectrin alpha subunit.
Yurchenco P, Speicher D, Morrow J, Knowles W, Marchesi V. Monoclonal antibodies as probes of domain structure of the spectrin alpha subunit. Journal Of Biological Chemistry 1982, 257: 9102-9107. PMID: 7096354, DOI: 10.1016/s0021-9258(18)34248-0.Peer-Reviewed Original Research
1980
Identification of proteolytically resistant domains of human erythrocyte spectrin.
Speicher D, Morrow J, Knowles W, Marchesi V. Identification of proteolytically resistant domains of human erythrocyte spectrin. Proceedings Of The National Academy Of Sciences Of The United States Of America 1980, 77: 5673-5677. PMID: 7003593, PMCID: PMC350131, DOI: 10.1073/pnas.77.10.5673.Peer-Reviewed Original Research